ID   A0A1Y2K3N5_9PROT        Unreviewed;       247 AA.
AC   A0A1Y2K3N5;
DT   30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT   30-AUG-2017, sequence version 1.
DT   27-MAR-2024, entry version 18.
DE   SubName: Full=Putative hydrolase {ECO:0000313|EMBL:OSM02287.1};
GN   ORFNames=MAIT1_02407 {ECO:0000313|EMBL:OSM02287.1};
OS   Magnetofaba australis IT-1.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Magnetococcales;
OC   Magnetococcaceae; Magnetofaba.
OX   NCBI_TaxID=1434232 {ECO:0000313|EMBL:OSM02287.1, ECO:0000313|Proteomes:UP000194003};
RN   [1] {ECO:0000313|EMBL:OSM02287.1, ECO:0000313|Proteomes:UP000194003}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IT-1 {ECO:0000313|EMBL:OSM02287.1,
RC   ECO:0000313|Proteomes:UP000194003};
RX   PubMed=27801294; DOI=10.1186/s12864-016-3064-9;
RA   Araujo A.C., Morillo V., Cypriano J., Teixeira L.C., Leao P., Lyra S.,
RA   Almeida L.G., Bazylinski D.A., Vasconcellos A.T., Abreu F., Lins U.;
RT   "Combined genomic and structural analyses of a cultured magnetotactic
RT   bacterium reveals its niche adaptation to a dynamic environment.";
RL   BMC Genomics 17:726-726(2016).
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|ARBA:ARBA00001946};
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:OSM02287.1}.
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DR   EMBL; LVJN01000020; OSM02287.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1Y2K3N5; -.
DR   STRING; 1434232.MAIT1_02407; -.
DR   OrthoDB; 148966at2; -.
DR   Proteomes; UP000194003; Unassembled WGS sequence.
DR   GO; GO:0016791; F:phosphatase activity; IEA:UniProt.
DR   GO; GO:0044249; P:cellular biosynthetic process; IEA:UniProt.
DR   GO; GO:1901566; P:organonitrogen compound biosynthetic process; IEA:UniProt.
DR   GO; GO:0044283; P:small molecule biosynthetic process; IEA:UniProt.
DR   Gene3D; 1.10.150.520; -; 1.
DR   Gene3D; 3.40.50.1000; HAD superfamily/HAD-like; 1.
DR   InterPro; IPR036412; HAD-like_sf.
DR   InterPro; IPR006439; HAD-SF_hydro_IA.
DR   InterPro; IPR023214; HAD_sf.
DR   NCBIfam; TIGR01549; HAD-SF-IA-v1; 1.
DR   NCBIfam; TIGR01509; HAD-SF-IA-v3; 1.
DR   PANTHER; PTHR46470; N-ACYLNEURAMINATE-9-PHOSPHATASE; 1.
DR   PANTHER; PTHR46470:SF2; N-ACYLNEURAMINATE-9-PHOSPHATASE; 1.
DR   Pfam; PF00702; Hydrolase; 1.
DR   PRINTS; PR00413; HADHALOGNASE.
DR   SFLD; SFLDG01129; C1.5:_HAD__Beta-PGM__Phosphata; 1.
DR   SFLD; SFLDS00003; Haloacid_Dehalogenase; 1.
DR   SUPFAM; SSF56784; HAD-like; 1.
PE   4: Predicted;
KW   Hydrolase {ECO:0000313|EMBL:OSM02287.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000194003}.
SQ   SEQUENCE   247 AA;  27282 MW;  257309E2C0FA5CCD CRC64;
     MALNIRNPEA FARKPAAVIF DTDNTLYDYA PAHAAASAAA REKAQALLGV DGDAFDDAYR
     AARKEVKARL GHVAASHSRL LYFQRMIERL GLKTQLLHTL DLNQTYWRTF LGASTLFPDA
     RALLEDLRAL SIHTAIVTDL TAEIQFRKIV YFDLADHFDY VVTSEEAGAD KPDLAPFQLA
     LEKLGLQAGE VWMVGDNAVN DIQGARALGI PCWQKLHTGV SEGQGEQAAD GTFTHFGEMR
     KFISVKF
//